Differential effects of ethanol and the rpsL1 (strA1) ribosomal mutation on the synthesis of an unusual protein coded by bacteriophages R17 and MS2 RNA

1981 ◽  
Vol 59 (10) ◽  
pp. 799-801 ◽  
Author(s):  
Michael Laughrea
Keyword(s):  
Ribosomal Protein ◽  
Protein Band ◽  
Detectable Effect ◽  
Related Protein ◽  
Differential Effects ◽  
Ribosomal Protein S12

During translation of R17 and MS2 RNA, ethanol stimulates the synthesis of a coat-related protein which has identical electrophotetic mobility to that of polypeptide 7 studied by Atkins and his colleagues. Streptomycin stimulates the synthesis of this polypeptide and broadens the protein band. In contrast the ribosomal protein S12 mutation rpsL1 (strA1) has no detectable effect on its synthesis.

scholarly journals Cloning and sequencing of mouse ribosomal protein S12 cDNA

1989 ◽  
Vol 17 (16) ◽  
pp. 6722-6722 ◽  
Author(s):  
Mohamed Ayane ◽  
Peter Nielsen ◽  
Georges Köhler
Keyword(s):  
Ribosomal Protein ◽  
Cloning And Sequencing ◽  
Ribosomal Protein S12

An intergenic G-rich region in Leishmania tarentolae kinetoplast maxicircle DNA is a pan-edited cryptogene encoding ribosomal protein S12

1992 ◽  
Vol 12 (1) ◽  
pp. 56-67
Author(s):  
D A Maslov ◽  
N R Sturm ◽  
B M Niner ◽  
E S Gruszynski ◽  
M Peris ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Sequence Similarity ◽  
Rich Region ◽  
Leishmania Tarentolae ◽  
Significant Sequence Similarity ◽  
The Family ◽  
Intergenic Regions ◽  
Ribosomal Protein S12

Six short G-rich intergenic regions in the maxicircle of Leishmania tarentolae are conserved in location and polarity in two other kinetoplastid species. We show here that G-rich region 6 (G6) represents a pan-edited cryptogene which contains at least two domains edited independently in a 3'-to-5' manner connected by short unedited regions. In the completely edited RNA, 117 uridines are added at 49 sites and 32 uridines are deleted at 13 sites, creating a translated 85-amino-acid polypeptide. Similar polypeptides are probably encoded by pan-edited G6 transcripts in two other species. The G6 polypeptide has significant sequence similarity to the family of S12 ribosomal proteins. A minicircle-encoded gRNA overlaps 12 editing sites in G6 mRNA, and chimeric gRNA/mRNA molecules were shown to exist, in agreement with the transesterification model for editing.

scholarly journals The enigma of the gene coding for ribosomal protein S12 in the chtoroplasts of Nicotiana

1986 ◽  
Vol 14 (2) ◽  
pp. 883-898 ◽  
Author(s):  
H. Fromm ◽  
M. Edelman ◽  
B. Koller ◽  
P. Goloubinoff ◽  
E. Galun
Keyword(s):  
Ribosomal Protein ◽  
Gene Coding ◽  
Ribosomal Protein S12

Expression in non-lens tissues of an enzyme activity related to the ‘lens-specific’ protein, delta crystallin

Development ◽  
1991 ◽  
Vol 111 (1) ◽  
pp. 181-190
Author(s):  
D.I. de Pomerai ◽  
W.K. Ip ◽  
M. McLaughlin ◽  
K.C. Perry
Keyword(s):  
Ectopic Expression ◽  
Molecular Size ◽  
Protein Band ◽  
Major Constituent ◽  
Lens Protein ◽  
Related Protein ◽  
Structural Protein ◽  
Cycle Enzyme ◽  
Published Evidence

When chick embryo neutral retina (NR) cells are cultured for long periods in vitro, they undergo extensive transdifferentiation into lens and express the lens protein, delta crystallin. We now demonstrate that this process is accompanied by a change in the chromatin conformation of the delta-gene locus from DNAase1-resistant to DNAase1-sensitive in the nuclei of most cells. Transcripts hybridising to a delta probe are also much more prevalent among the in vitro transcription products from lens or transdifferentiated NR culture nuclei, as compared to nuclei from fresh NR tissue. Published evidence indicates that the chick delta 1 crystallin gene encodes the major structural protein of embryonic lens fibres, whereas the closely related delta 2 gene may encode the urea-cycle enzyme argininosuccinate lyase (ASL). Our present data lends further support to this view. Both immunodetectable delta-related protein(s) and ASL activity are present in fresh embryonic NR tissue, as well as in mouse and Rana liver, and in Rana lens. Our polyclonal anti-delta antibody also cross-reacts with a major constituent of commercial bovine ASL, of the same molecular size as chick delta crystallin. Immunoselection studies suggest that the ASL activity in chick embryonic NR is conferred mainly by the delta-related protein band. So-called ‘ectopic’ expression of delta crystallin in embryonic NR (and other tissues) may thus involve the delta 2/ASL gene, and could reflect some metabolic requirement for ASL activity.

Modulation of 16S rRNA function by ribosomal protein S12

2007 ◽  
Vol 1769 (7-8) ◽  
pp. 462-471 ◽  
Author(s):  
Anton Vila-Sanjurjo ◽  
Ying Lu ◽  
Jamie L. Aragonez ◽  
Rebekah E. Starkweather ◽  
Manoj Sasikumar ◽  
...  
Keyword(s):  
16S Rrna ◽  
Ribosomal Protein ◽  
Ribosomal Protein S12

scholarly journals Severity of the Streptomycin Resistance and Streptomycin Dependence Phenotypes of Ribosomal Protein S12 of Thermus thermophilus Depends on the Identity of Highly Conserved Amino Acid Residues

2005 ◽  
Vol 187 (10) ◽  
pp. 3548-3550 ◽  
Author(s):  
Jennifer F. Carr ◽  
Steven T. Gregory ◽  
Albert E. Dahlberg
Keyword(s):  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Gene Replacement ◽  
Streptomycin Resistance ◽  
Site Directed Mutagenesis ◽  
Structural Basis ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Drug Dependent ◽  
Ribosomal Protein S12

ABSTRACT The structural basis for the streptomycin dependence phenotype of ribosomal protein S12 mutants is poorly understood. Here we describe the application of site-directed mutagenesis and gene replacement of Thermus thermophilus rpsL to assess the importance of side chain identity and tertiary interactions as phenotypic determinants of drug-dependent mutants.

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